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  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2003-08-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stock, Joann -- New York, N.Y. -- Science. 2003 Aug 22;301(5636):1059-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Seismo Lab, California Institute of Technology, Pasadena, CA 91125, USA. jstock@gps.caltech.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12934000" target="_blank"〉PubMed〈/a〉
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-09-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stock, Joann M -- New York, N.Y. -- Science. 2006 Sep 1;313(5791):1250-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Geological and Planetary Sciences, California Institute of Technology, Pasadena, CA 91125, USA. jstock@gps.caltech.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16946060" target="_blank"〉PubMed〈/a〉
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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-12-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉ter Meulen, Volker -- Stock, Gunter -- New York, N.Y. -- Science. 2010 Dec 10;330(6010):1455. doi: 10.1126/science.1200095.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21148355" target="_blank"〉PubMed〈/a〉
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  • 4
    Publication Date: 2012-07-24
    Description: Seismological observations of the 2012 moment magnitude 8.6 Sumatra earthquake reveal unprecedented complexity of dynamic rupture. The surprisingly large magnitude results from the combination of deep extent, high stress drop, and rupture of multiple faults. Back-projection source imaging indicates that the rupture occurred on distinct planes in an orthogonal conjugate fault system, with relatively slow rupture speed. The east-southeast-west-northwest ruptures add a new dimension to the seismotectonics of the Wharton Basin, which was previously thought to be controlled by north-south strike-slip faulting. The rupture turned twice into the compressive quadrant, against the preferred branching direction predicted by dynamic Coulomb stress calculations. Orthogonal faulting and compressional branching indicate that rupture was controlled by a pressure-insensitive strength of the deep oceanic lithosphere.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meng, L -- Ampuero, J-P -- Stock, J -- Duputel, Z -- Luo, Y -- Tsai, V C -- New York, N.Y. -- Science. 2012 Aug 10;337(6095):724-6. doi: 10.1126/science.1224030. Epub 2012 Jul 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Seismological Laboratory, Division of Geological and Planetary Sciences, California Institute of Technology, Pasadena, CA 91125, USA. lsmeng@gps.caltech.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22821986" target="_blank"〉PubMed〈/a〉
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  • 5
    Publication Date: 1993-04-09
    Description: The Landers earthquake, which had a moment magnitude (M(w)) of 7.3, was the largest earthquake to strike the contiguous United States in 40 years. This earthquake resulted from the rupture of five major and many minor right-lateral faults near the southern end of the eastern California shear zone, just north of the San Andreas fault. Its M(w) 6.1 preshock and M(w) 6.2 aftershock had their own aftershocks and foreshocks. Surficial geological observations are consistent with local and far-field seismologic observations of the earthquake. Large surficial offsets (as great as 6 meters) and a relatively short rupture length (85 kilometers) are consistent with seismological calculations of a high stress drop (200 bars), which is in turn consistent with an apparently long recurrence interval for these faults.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sieh, K -- Jones, L -- Hauksson, E -- Hudnut, K -- Eberhart-Phillips, D -- Heaton, T -- Hough, S -- Hutton, K -- Kanamori, H -- Lilje, A -- Lindvall, S -- McGill, S F -- Mori, J -- Rubin, C -- Spotila, J A -- Stock, J -- Thio, H K -- Treiman, J -- Wernicke, B -- Zachariasen, J -- New York, N.Y. -- Science. 1993 Apr 9;260(5105):171-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17807175" target="_blank"〉PubMed〈/a〉
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  • 6
    Publication Date: 1993-02-12
    Description: In human neutrophils, as in other cell types, Ras-related guanosine triphosphate-binding proteins are directed toward their regulatory targets in membranes by a series of posttranslational modifications that include methyl esterification of a carboxyl-terminal prenylcysteine residue. In intact cells and in a reconstituted in vitro system, the amount of carboxyl methylation of Ras-related proteins increased in response to the chemoattractant N-formyl-methionyl-leucyl-phenylalanine (FMLP). Activation of Ras-related proteins by guanosine-5'-O-(3-thiotriphosphate) had a similar effect and induced translocation of p22rac2 from cytosol to plasma membrane. Inhibitors of prenylcysteine carboxyl methylation effectively blocked neutrophil responses to FMLP. These findings suggest a direct link between receptor-mediated signal transduction and the carboxyl methylation of Ras-related proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Philips, M R -- Pillinger, M H -- Staud, R -- Volker, C -- Rosenfeld, M G -- Weissmann, G -- Stock, J B -- AR-07176-18/AR/NIAMS NIH HHS/ -- GM 20277/GM/NIGMS NIH HHS/ -- GM-8309/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1993 Feb 12;259(5097):977-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, New York University Medical Center, NY 10016.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8438158" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Membrane/metabolism ; Cytosol/metabolism ; GTP-Binding Proteins/*metabolism ; *Guanine Nucleotide Dissociation Inhibitors ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Guanosine Triphosphate/pharmacology ; Humans ; Methionine/analogs & derivatives/metabolism ; Methylation ; N-Formylmethionine Leucyl-Phenylalanine/pharmacology ; Neutrophils/*physiology ; Protein Methyltransferases/metabolism ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins p21(ras)/metabolism ; S-Adenosylmethionine/metabolism ; Signal Transduction/*physiology ; Tritium ; rap GTP-Binding Proteins ; rho-Specific Guanine Nucleotide Dissociation Inhibitors
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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-11-27
    Description: Adenosine triphosphate (ATP) synthase contains a rotary motor involved in biological energy conversion. Its membrane-embedded F0 sector has a rotation generator fueled by the proton-motive force, which provides the energy required for the synthesis of ATP by the F1 domain. An electron density map obtained from crystals of a subcomplex of yeast mitochondrial ATP synthase shows a ring of 10 c subunits. Each c subunit forms an alpha-helical hairpin. The interhelical loops of six to seven of the c subunits are in close contact with the gamma and delta subunits of the central stalk. The extensive contact between the c ring and the stalk suggests that they may rotate as an ensemble during catalysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stock, D -- Leslie, A G -- Walker, J E -- New York, N.Y. -- Science. 1999 Nov 26;286(5445):1700-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge CB2 2XY, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10576729" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Catalysis ; Crystallization ; Crystallography, X-Ray ; Hydrogen Bonding ; Mitochondria/enzymology ; Models, Molecular ; Molecular Motor Proteins/*chemistry/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Proton-Motive Force ; Proton-Translocating ATPases/*chemistry/metabolism ; Protons ; Saccharomyces cerevisiae/enzymology
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  • 8
    Publication Date: 1997-12-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kang, S M -- Hoffmann, A -- Le, D -- Springer, M L -- Stock, P G -- Blau, H M -- F32 HL08991/HL/NHLBI NIH HHS/ -- R01-CA59717/CA/NCI NIH HHS/ -- R01-HD18179/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1997 Nov 14;278(5341):1322-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9411754" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD95/biosynthesis ; Apoptosis ; Cell Differentiation ; Cell Transplantation ; Fas Ligand Protein ; *Graft Rejection ; Immune Tolerance ; Islets of Langerhans/cytology ; *Islets of Langerhans Transplantation ; Membrane Glycoproteins/genetics/*physiology ; Mice ; Mice, Inbred C3H ; Mice, Inbred C57BL ; Muscle Fibers, Skeletal/*cytology/metabolism ; Muscle, Skeletal/*cytology/metabolism ; Neutrophils/*immunology ; Transfection
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  • 9
    Publication Date: 2000-03-04
    Description: Members of the cytochrome P450 superfamily catalyze the addition of molecular oxygen to nonactivated hydrocarbons at physiological temperature-a reaction that requires high temperature to proceed in the absence of a catalyst. Structures were obtained for three intermediates in the hydroxylation reaction of camphor by P450cam with trapping techniques and cryocrystallography. The structure of the ferrous dioxygen adduct of P450cam was determined with 0.91 angstrom wavelength x-rays; irradiation with 1.5 angstrom x-rays results in breakdown of the dioxygen molecule to an intermediate that would be consistent with an oxyferryl species. The structures show conformational changes in several important residues and reveal a network of bound water molecules that may provide the protons needed for the reaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schlichting, I -- Berendzen, J -- Chu, K -- Stock, A M -- Maves, S A -- Benson, D E -- Sweet, R M -- Ringe, D -- Petsko, G A -- Sligar, S G -- GM31756/GM/NIGMS NIH HHS/ -- GM33775/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Mar 3;287(5458):1615-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Institute for Molecular Physiology, Department of Physical Biochemistry, Otto Hahn Strasse 11, 44227 Dortmund, Germany. ilme.schlichting@mpi-dortmund.mpg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10698731" target="_blank"〉PubMed〈/a〉
    Keywords: Camphor/*chemistry/*metabolism ; Camphor 5-Monooxygenase/*chemistry/*metabolism ; Catalysis ; Crystallization ; Crystallography, X-Ray ; Electrons ; Ferric Compounds/chemistry/metabolism ; Ferrous Compounds/chemistry/metabolism ; Hydrogen Bonding ; Hydroxylation ; Ligands ; Models, Molecular ; Molecular Conformation ; Oxygen/chemistry/metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protons ; Pseudomonas putida/enzymology ; Water/chemistry/metabolism
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  • 10
    Publication Date: 2010-03-06
    Description: Nuclear collisions recreate conditions in the universe microseconds after the Big Bang. Only a very small fraction of the emitted fragments are light nuclei, but these states are of fundamental interest. We report the observation of antihypertritons--comprising an antiproton, an antineutron, and an antilambda hyperon--produced by colliding gold nuclei at high energy. Our analysis yields 70 +/- 17 antihypertritons ((Lambda)(3)-H) and 157 +/- 30 hypertritons (Lambda3H). The measured yields of Lambda3H ((Lambda)(3)-H) and 3He (3He) are similar, suggesting an equilibrium in coordinate and momentum space populations of up, down, and strange quarks and antiquarks, unlike the pattern observed at lower collision energies. The production and properties of antinuclei, and of nuclei containing strange quarks, have implications spanning nuclear and particle physics, astrophysics, and cosmology.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉STAR Collaboration -- Abelev, B I -- Aggarwal, M M -- Ahammed, Z -- Alakhverdyants, A V -- Alekseev, I -- Anderson, B D -- Arkhipkin, D -- Averichev, G S -- Balewski, J -- Barnby, L S -- Baumgart, S -- Beavis, D R -- Bellwied, R -- Betancourt, M J -- Betts, R R -- Bhasin, A -- Bhati, A K -- Bichsel, H -- Bielcik, J -- Bielcikova, J -- Biritz, B -- Bland, L C -- Bonner, B E -- Bouchet, J -- Braidot, E -- Brandin, A V -- Bridgeman, A -- Bruna, E -- Bueltmann, S -- Bunzarov, I -- Burton, T P -- Cai, X Z -- Caines, H -- Calderon, M -- Catu, O -- Cebra, D -- Cendejas, R -- Cervantes, M C -- Chajecki, Z -- Chaloupka, P -- Chattopadhyay, S -- Chen, H F -- Chen, J H -- Chen, J Y -- Cheng, J -- Cherney, M -- Chikanian, A -- Choi, K E -- Christie, W -- Chung, P -- Clarke, R F -- Codrington, M J M -- Corliss, R -- Cramer, J G -- Crawford, H J -- Das, D -- Dash, S -- Davila Leyva, A -- De Silva, L C -- Debbe, R R -- Dedovich, T G -- DePhillips, M -- Derevschikov, A A -- Derradi de Souza, R -- Didenko, L -- Djawotho, P -- Dogra, S M -- Dong, X -- Drachenberg, J L -- Draper, J E -- Dunlop, J C -- Dutta Mazumdar, M R -- Efimov, L G -- Elhalhuli, E -- Elnimr, M -- Engelage, J -- Eppley, G -- Erazmus, B -- Estienne, M -- Eun, L -- Evdokimov, O -- Fachini, P -- Fatemi, R -- Fedorisin, J -- Fersch, R G -- Filip, P -- Finch, E -- Fine, V -- Fisyak, Y -- Gagliardi, C A -- Gangadharan, D R -- Ganti, M S -- Garcia-Solis, E J -- Geromitsos, A -- Geurts, F -- Ghazikhanian, V -- Ghosh, P -- Gorbunov, Y N -- Gordon, A -- Grebenyuk, O -- Grosnick, D -- Grube, B -- Guertin, S M -- Gupta, A -- Gupta, N -- Guryn, W -- Haag, B -- Hamed, A -- Han, L-X -- Harris, J W -- Hays-Wehle, J P -- Heinz, M -- Heppelmann, S -- Hirsch, A -- Hjort, E -- Hoffman, A M -- Hoffmann, G W -- Hofman, D J -- Hollis, R S -- Huang, B -- Huang, H Z -- Humanic, T J -- Huo, L -- Igo, G -- Iordanova, A -- Jacobs, P -- Jacobs, W W -- Jakl, P -- Jena, C -- Jin, F -- Jones, C L -- Jones, P G -- Joseph, J -- Judd, E G -- Kabana, S -- Kajimoto, K -- Kang, K -- Kapitan, J -- Kauder, K -- Keane, D -- Kechechyan, A -- Kettler, D -- Kikola, D P -- Kiryluk, J -- Kisiel, A -- Klein, S R -- Knospe, A G -- Kocoloski, A -- Koetke, D D -- Kollegger, T -- Konzer, J -- Kopytine, M -- Koralt, I -- Koroleva, L -- Korsch, W -- Kotchenda, L -- Kouchpil, V -- Kravtsov, P -- Krueger, K -- Krus, M -- Kumar, L -- Kurnadi, P -- Lamont, M A C -- Landgraf, J M -- LaPointe, S -- Lauret, J -- Lebedev, A -- Lednicky, R -- Lee, C-H -- Lee, J H -- Leight, W -- Levine, M J -- Li, C -- Li, L -- Li, N -- Li, W -- Li, X -- Li, Y -- Li, Z -- Lin, G -- Lindenbaum, S J -- Lisa, M A -- Liu, F -- Liu, H -- Liu, J -- Ljubicic, T -- Llope, W J -- Longacre, R S -- Love, W A -- Lu, Y -- Luo, X -- Ma, G L -- Ma, Y G -- Mahapatra, D P -- Majka, R -- Mal, O I -- Mangotra, L K -- Manweiler, R -- Margetis, S -- Markert, C -- Masui, H -- Matis, H S -- Matulenko, Yu A -- McDonald, D -- McShane, T S -- Meschanin, A -- Milner, R -- Minaev, N G -- Mioduszewski, S -- Mischke, A -- Mitrovski, M K -- Mohanty, B -- Mondal, M M -- Morozov, B -- Morozov, D A -- Munhoz, M G -- Nandi, B K -- Nattrass, C -- Nayak, T K -- Nelson, J M -- Netrakanti, P K -- Ng, M J -- Nogach, L V -- Nurushev, S B -- Odyniec, G -- Ogawa, A -- Okada, H -- Okorokov, V -- Olson, D -- Pachr, M -- Page, B S -- Pal, S K -- Pandit, Y -- Panebratsev, Y -- Pawlak, T -- Peitzmann, T -- Perevoztchikov, V -- Perkins, C -- Peryt, W -- Phatak, S C -- Pile, P -- Planinic, M -- Ploskon, M A -- Pluta, J -- Plyku, D -- Poljak, N -- Poskanzer, A M -- Potukuchi, B V K S -- Powell, C B -- Prindle, D -- Pruneau, C -- Pruthi, N K -- Pujahari, P R -- Putschke, J -- Qiu, H -- Raniwala, R -- Raniwala, S -- Ray, R L -- Redwine, R -- Reed, R -- Ritter, H G -- Roberts, J B -- Rogachevskiy, O V -- Romero, J L -- Rose, A -- Roy, C -- Ruan, L -- Sahoo, R -- Sakai, S -- Sakrejda, I -- Sakuma, T -- Salur, S -- Sandweiss, J -- Sangaline, E -- Schambach, J -- Scharenberg, R P -- Schmitz, N -- Schuster, T R -- Seele, J -- Seger, J -- Selyuzhenkov, I -- Seyboth, P -- Shahaliev, E -- Shao, M -- Sharma, M -- Shi, S S -- Sichtermann, E P -- Simon, F -- Singaraju, R N -- Skoby, M J -- Smirnov, N -- Sorensen, P -- Sowinski, J -- Spinka, H M -- Srivastava, B -- Stanislaus, T D S -- Staszak, D -- Stevens, J R -- Stock, R -- Strikhanov, M -- Stringfellow, B -- Suaide, A A P -- Suarez, M C -- Subba, N L -- Sumbera, M -- Sun, X M -- Sun, Y -- Sun, Z -- Surrow, B -- Svirida, D N -- Symons, T J M -- Szanto de Toledo, A -- Takahashi, J -- Tang, A H -- Tang, Z -- Tarini, L H -- Tarnowsky, T -- Thein, D -- Thomas, J H -- Tian, J -- Timmins, A R -- Timoshenko, S -- Tlusty, D -- Tokarev, M -- Trainor, T A -- Tram, V N -- Trentalange, S -- Tribble, R E -- Tsai, O D -- Ulery, J -- Ullrich, T -- Underwood, D G -- Van Buren, G -- van Leeuwen, M -- van Nieuwenhuizen, G -- Vanfossen, J A Jr -- Varma, R -- Vasconcelos, G M S -- Vasiliev, A N -- Videbaek, F -- Viyogi, Y P -- Vokal, S -- Voloshin, S A -- Wada, M -- Walker, M -- Wang, F -- Wang, G -- Wang, H -- Wang, J S -- Wang, Q -- Wang, X L -- Wang, Y -- Webb, G -- Webb, J C -- Westfall, G D -- Whitten, C Jr -- Wieman, H -- Wingfield, E -- Wissink, S W -- Witt, R -- Wu, Y -- Xie, W -- Xu, H -- Xu, N -- Xu, Q H -- Xu, W -- Xu, Y -- Xu, Z -- Xue, L -- Yang, Y -- Yepes, P -- Yip, K -- Yoo, I-K -- Yue, Q -- Zawisza, M -- Zbroszczyk, H -- Zhan, W -- Zhang, J -- Zhang, S -- Zhang, W M -- Zhang, X P -- Zhang, Y -- Zhang, Z P -- Zhao, J -- Zhong, C -- Zhou, J -- Zhou, W -- Zhu, X -- Zhu, Y H -- Zoulkarneev, R -- Zoulkarneeva, Y -- New York, N.Y. -- Science. 2010 Apr 2;328(5974):58-62. doi: 10.1126/science.1183980. Epub 2010 Mar 4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20203011" target="_blank"〉PubMed〈/a〉
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